Martin-Luther-Universität Halle-Wittenberg

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1981-1985



1981


Bernhardt, G., Rudolph, R. & Jaenicke, R. (1981)
Z. Naturforsch. 36c, 772-777
Reassociation of Lactic Dehydrogenase from Pig Heart Studied by Crosslinking with Glutaraldehyde.

Herrmann, R., Jaenicke, R. & Rudolph, R. (1981)
Biochemistry 20, 5195-5201
Analysis of the Reconstitution of Oligomeric Enzymes by Crosslinking with Glutaraldehyde: Kinetics of Reassociation of Lactic Dehydrogenase.

Jaenicke, R., Vogel, W. & Rudolph, R. (1981)
Eur. J. Biochem. 114, 525-531
Dimeric Intermediates in the Dissociation of Lactic Dehydrogenase.

Girg, R., Rudolph, R. & Jaenicke, R. (1981)
Eur. J. Biochem. 119, 301-305
Limited Proteolysis of Porcine Muscle Lactic Dehydrogenase by Thermolysin during Reconstitution Yields Dimers.

Zettlmeißl, G., Rudolph, R. & Jaenicke, R. (1981)
Eur. J. Biochem. 121, 169-175
Reconstitution of Lactic Dehydrogenase after Acid Dissociation. The Yield of Reactivation is Determined by Conformational Rearrangements of the Dissociated Monomers.

Jaenicke, R., Rudolph, R. & Heider, I. (1981)
Biochem. Int. 2, 23-31
Specificity in the Subunit Assembly of Oligomeric Enzymes.

1982


Zettlmeißl, G., Rudolph, R. & Jaenicke, R. (1982)
Eur. J. Biochem. 125, 605-608
The Yield of Reactivation of Lactic Dehydrogenase after Guani­dineHCl Denaturation is Not Determined by Proline cis/trans Isomerization.

Zettlmeißl, Rudolph, R. & Jaenicke, R. (1982)
Biochemistry 21, 3946-3950
Rate-Determining Folding and Association Reactions on the Reconstitution Pathway of Porcine Skeletal Muscle Lactic Dehydrogenase after Denaturation by Guanidine Hydrochloride.

Stimson, E.R., Montelione, G.T., Meinwald, Y.C., Rudolph, R.K.E. & Scheraga, H.A. (1982)
Biochemistry 21, 5252-5262
Equilibrium Ratios of cis- and trans-Proline Conformers in Fragments of Ribonuclease A from Nuclear Magnetic Resonance Spectra of Adjacent Tyrosine Ring Resonances.

Hermann, R., Rudolph, R. & Jaenicke, R. (1982)
Hoppe-Seyler`s Z. Physiol. Chem. 363, 1259-1265
The Use of Subunit Hybridization to Monitor the Reassociation of Porcine Lactate Dehydrogenase after Acid Dissociation.

1983


Rudolph, R., Bohrer, M. & Fischer, S. (1983)
Eur. J. Biochem. 131, 383-386
Physicochemical Characterization of a Fast Refolding Monomeric Class I Fructose-1,6-Bisphosphate Aldolase from Staphylococcus aureus.

Rudolph, R. & Fuchs, I. (1983)
Hoppe-Seyler`s Z. Physiol. Chem. 364, 813-820
Influence of Glutathione on the Reactivation of Enzymes Containing Cysteine or Cystine.

Hermann, R., Rudolph, R., Jaenicke, R., Price, N.C. & Scobbie, A. (1983)
J. Biol. Chem. 258, 11014-11019
The Reconstitution of Denatured Phosphoglycerate Mutase.

Girg, R., Jaenicke, R. & Rudolph, R. (1983)
Biochem. Int. 7, 433-441
Dimers of Porcine Skeletal Muscle Lactate Dehydrogenase Produced by Limited Proteolysis during Reassociation are Enzymatically Active in the Presence of Stabilizing Salt.

Girg, R., Rudolph, R. & Jaenicke, R. (1983)
FEBS-Lett. 163, 132-135
The Dimeric Intermediate on the Pathway of Reconstitution of Lactate Dehydrogenase is Enzymatically Active.

Zettlmeißl, G., Rudolph, R. & Jaenicke, R. (1983)
Arch. Biochem. Biophys. 224, 161-168
Limited Proteolysis as a Tool to Study the Kinetics of Protein Folding: Conformational Rearrangements in Acid-Dissociated Lactic Dehydrogenase as Determined by Pepsin Digestion.

Jaenicke, R. & Rudolph, R. (1983)
"Biological Oxidations", 34. Colloquium Mosbach (Sund, H. & Ullrich, V., eds) pp. 62-90, Springer, Berlin, Heidelberg
What NAD-Dependent Dehydrogenases Teach Us About the Folding and Association of Oligomeric Proteins.

1984


Zettlmeißl, G., Teschner, W., Rudolph, R., Jaenicke, R. & Gäde, G.
(1984)
Eur. J. Biochem. 143, 401-407
Isolation, Physicochemical Properties, and Folding of Octopine Dehydrogenase from Pecten jacobaeus.

1985

Rudolph, R. (1985)
Biochem. Soc. Trans. 13, 308-311
The Use of Limited Proteolysis in Studies on Protein Folding and Association.Gerl, M., Rudolph, R. & Jaenicke, R. (1985)
Biol. Chem. Hoppe-Seyler 366, 447-454
Mechanism and Specificity of Reconstitution of Dimeric Lactate Dehydrogenase from Limulus polyphemus.

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